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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

A β-Peptide Agonist of the GLP-1 Receptor, a Class B GPCR
Elizabeth V. Denton, Cody J. Craig, Rebecca L. Pongratz, et al.
Organic Letters (2013) Vol. 15, Iss. 20, pp. 5318-5321
Open Access | Times Cited: 39

Showing 1-25 of 39 citing articles:

Peptides Containing β-Amino Acid Patterns: Challenges and Successes in Medicinal Chemistry
Chiara Cabrele, Tamás A. Martinek, Oliver Reiser, et al.
Journal of Medicinal Chemistry (2014) Vol. 57, Iss. 23, pp. 9718-9739
Open Access | Times Cited: 300
Modulating protein–protein interactions: the potential of peptides
Laura Nevola, Ernest Giralt
Chemical Communications (2014) Vol. 51, Iss. 16, pp. 3302-3315
Closed Access | Times Cited: 276
Discovery and characterization of smORF-encoded bioactive polypeptides
Alan Saghatelian, Juan Pablo Couso
Nature Chemical Biology (2015) Vol. 11, Iss. 12, pp. 909-916
Open Access | Times Cited: 249
Glucagon-like Peptide-1 (GLP-1) Analogs: Recent Advances, New Possibilities, and Therapeutic Implications
Bikash Manandhar, Jung‐Mo Ahn
Journal of Medicinal Chemistry (2014) Vol. 58, Iss. 3, pp. 1020-1037
Open Access | Times Cited: 169
Backbone modification of a polypeptide drug alters duration of action in vivo
Ross W. Cheloha, Akira Maeda, Thomas Dean, et al.
Nature Biotechnology (2014) Vol. 32, Iss. 7, pp. 653-655
Open Access | Times Cited: 115
A Potent α/β-Peptide Analogue of GLP-1 with Prolonged Action in Vivo
Lisa M. Johnson, Stacey Barrick, Marlies V. Hager, et al.
Journal of the American Chemical Society (2014) Vol. 136, Iss. 37, pp. 12848-12851
Open Access | Times Cited: 94
Targeting recognition surfaces on natural proteins with peptidic foldamers
James W. Checco, Samuel H. Gellman
Current Opinion in Structural Biology (2016) Vol. 39, pp. 96-105
Open Access | Times Cited: 81
β-Arrestin-Biased Agonists of the GLP-1 Receptor from β-Amino Acid Residue Incorporation into GLP-1 Analogues
Marlies V. Hager, Lisa M. Johnson, Denise Wootten, et al.
Journal of the American Chemical Society (2016) Vol. 138, Iss. 45, pp. 14970-14979
Open Access | Times Cited: 78
Transmembrane signal transduction by peptide hormones via family B G protein-coupled receptors
Kelly J. Culhane, Yuting Liu, Yingying Cai, et al.
Frontiers in Pharmacology (2015) Vol. 6
Open Access | Times Cited: 69
Foldamer-mediated manipulation of a pre-amyloid toxin
Sunil Kumar, Melissa Birol, Diana E. Schlamadinger, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 67
Bent into shape: Folded peptides to mimic protein structure and modulate protein function
Haley I. Merritt, Nicholas Sawyer, Paramjit S. Arora
Peptide Science (2020) Vol. 112, Iss. 1
Open Access | Times Cited: 57
Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1
Marlies V. Hager, Lachlan Clydesdale, Samuel H. Gellman, et al.
Biochemical Pharmacology (2017) Vol. 136, pp. 99-108
Open Access | Times Cited: 56
Peptide-oligourea hybrids analogue of GLP-1 with improved action in vivo
Juliette Frémaux, Claire Venin, Laura Mauran, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 47
Effects of Single α-to-β Residue Replacements on Structure and Stability in a Small Protein: Insights from Quasiracemic Crystallization
Dale F. Kreitler, D.E. Mortenson, Katrina T. Forest, et al.
Journal of the American Chemical Society (2016) Vol. 138, Iss. 20, pp. 6498-6505
Open Access | Times Cited: 41
Positive Allostery in Metal Ion Binding by a Cooperatively Folded β-Peptide Bundle
Jonathan P. Miller, Michael S. Melicher, Alanna Schepartz
Journal of the American Chemical Society (2014) Vol. 136, Iss. 42, pp. 14726-14729
Open Access | Times Cited: 35
13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint
Claire M. Grison, Sylvie Robin, David J. Aitken
Chemical Communications (2016) Vol. 52, Iss. 50, pp. 7802-7805
Open Access | Times Cited: 33
Backbone extension acyl rearrangements enable cellular synthesis of proteins with internal β2-peptide linkages
Leah T. Roe, Carly K. Schissel, Taylor L. Dover, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 10
Foldamer scaffolds suggest distinct structures are associated with alternative gains-of-function in a preamyloid toxin
Sunil Kumar, Melissa Birol, Andrew D. Miranker
Chemical Communications (2016) Vol. 52, Iss. 38, pp. 6391-6394
Open Access | Times Cited: 25
Development of Potent, Protease-Resistant Agonists of the Parathyroid Hormone Receptor with Broad β Residue Distribution
Ross W. Cheloha, Bingming Chen, Niyanta N. Kumar, et al.
Journal of Medicinal Chemistry (2017) Vol. 60, Iss. 21, pp. 8816-8833
Open Access | Times Cited: 20
Controlling the Helix Handedness of ααβ‐Peptide Foldamers through Sequence Shifting
Monika Szefczyk, Ewelina Węglarz‐Tomczak, Paulina Fortuna, et al.
Angewandte Chemie International Edition (2017) Vol. 56, Iss. 8, pp. 2087-2091
Closed Access | Times Cited: 19
Hydrocarbon-Stitched Peptide Agonists of Glucagon-Like Peptide-1 Receptor
Gregory H. Bird, Accalia Fu, Silvia Escudero, et al.
ACS Chemical Biology (2020) Vol. 15, Iss. 6, pp. 1340-1348
Open Access | Times Cited: 16
Rotamer Libraries for the High-Resolution Design of β-Amino Acid Foldamers
Andrew M. Watkins, Timothy W. Craven, P. Douglas Renfrew, et al.
Structure (2017) Vol. 25, Iss. 11, pp. 1771-1780.e3
Open Access | Times Cited: 16
Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation
Imane Nekkaa, Dóra Bogdán, Tamás Gáti, et al.
Chemical Communications (2019) Vol. 55, Iss. 21, pp. 3061-3064
Closed Access | Times Cited: 14
Systematic ‘foldamerization’ of peptide inhibiting p53-MDM2/X interactions by the incorporation of trans- or cis-2-aminocyclopentanecarboxylic acid residues
Paulina Fortuna, Aleksandra Twarda‐Clapa, Łukasz Skalniak, et al.
European Journal of Medicinal Chemistry (2020) Vol. 208, pp. 112814-112814
Closed Access | Times Cited: 14
Drug discovery approaches targeting the incretin pathway
Xinxian Deng, Mojdeh S. Tavallaie, Ran Sun, et al.
Bioorganic Chemistry (2020) Vol. 99, pp. 103810-103810
Closed Access | Times Cited: 13
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